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Small archaeal modifier protein 2 (SAMP2) (Ubiquitin-like small archaeal modifier protein 2)

 SAMP2_PYRFU             Reviewed;          69 AA.
Q8U1Z3;
25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
20-DEC-2017, entry version 79.
RecName: Full=Small archaeal modifier protein 2 {ECO:0000303|PubMed:28479062};
Short=SAMP2 {ECO:0000303|PubMed:28479062};
AltName: Full=Ubiquitin-like small archaeal modifier protein 2 {ECO:0000303|PubMed:28479062};
Name=samp2 {ECO:0000303|PubMed:28479062};
OrderedLocusNames=PF1061 {ECO:0000312|EMBL:AAL81185.1};
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=186497;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
{ECO:0000312|Proteomes:UP000001013};
PubMed=10430560;
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
DiRuggiero J., Robb F.T.;
"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
P. horikoshii inferred from complete genomic sequences.";
Genetics 152:1299-1305(1999).
[2] {ECO:0000244|PDB:1RWS, ECO:0000244|PDB:1SF0}
STRUCTURE BY NMR OF 2-69.
PubMed=15704012; DOI=10.1007/s10969-005-4899-5;
Valafar H., Mayer K.L., Bougault C.M., LeBlond P.D., Jenney F.E.,
Brereton P.S., Adams M.W., Prestegard J.H.;
"Backbone solution structures of proteins using residual dipolar
couplings: application to a novel structural genomics target.";
J. Struct. Funct. Genomics 5:241-254(2004).
[3] {ECO:0000244|PDB:5LDA}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PFJAMM1
PROTEIN, AND FUNCTION.
PubMed=28479062; DOI=10.1016/j.str.2017.04.002;
Cao S., Engilberge S., Girard E., Gabel F., Franzetti B.,
Maupin-Furlow J.A.;
"Structural insight into ubiquitin-like protein recognition and
oligomeric states of JAMM/MPN+ proteases.";
Structure 25:823-833(2017).
-!- FUNCTION: Functions as a protein modifier covalently attached to
lysine residues of substrate proteins, as well as a sulfur carrier
in tRNA thiolation. The protein modification process is termed
sampylation and involves the formation of an isopeptide bond
between the SAMP2 C-terminal glycine carboxylate and the epsilon-
amino group of lysine residues on target proteins. Is able to form
polymeric chains with itself likely at Lys-55, similar to
ubiquitin and other ubiquitin-like proteins. May serve as a
proteolytic signal in the cell to target proteins for degradation
by proteasomes. {ECO:0000250|UniProtKB:D4GZE7,
ECO:0000305|PubMed:15704012}.
-!- PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by
UbaA, and also probably thiocarboxylated (-COSH) to function in
sulfur transfer. {ECO:0000250|UniProtKB:D4GZE7}.
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EMBL; AE009950; AAL81185.1; -; Genomic_DNA.
PDB; 1RWS; NMR; -; A=2-69.
PDB; 1SF0; NMR; -; A=2-69.
PDB; 5LDA; X-ray; 1.90 A; B=1-69.
PDBsum; 1RWS; -.
PDBsum; 1SF0; -.
PDBsum; 5LDA; -.
ProteinModelPortal; Q8U1Z3; -.
SMR; Q8U1Z3; -.
STRING; 186497.PF1061; -.
PRIDE; Q8U1Z3; -.
EnsemblBacteria; AAL81185; AAL81185; PF1061.
KEGG; pfu:PF1061; -.
PATRIC; fig|186497.12.peg.1122; -.
eggNOG; arCOG00535; Archaea.
eggNOG; COG2104; LUCA.
HOGENOM; HOG000232261; -.
KO; K03154; -.
OMA; EIEWREG; -.
OrthoDB; POG093Z0OCI; -.
EvolutionaryTrace; Q8U1Z3; -.
Proteomes; UP000001013; Chromosome.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
InterPro; IPR003749; ThiS/MoaD-like.
Pfam; PF02597; ThiS; 1.
SUPFAM; SSF54285; SSF54285; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Isopeptide bond; Nucleotide-binding;
Phosphoprotein; Reference proteome; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 69 Small archaeal modifier protein 2.
/FTId=PRO_0000441761.
MOD_RES 69 69 1-thioglycine; alternate.
{ECO:0000250|UniProtKB:D4GZE7}.
MOD_RES 69 69 Glycyl adenylate; alternate.
{ECO:0000250|UniProtKB:D4GZE7}.
CROSSLNK 55 55 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SAMP2).
{ECO:0000250|UniProtKB:D4GZE7}.
CROSSLNK 69 69 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins); alternate.
{ECO:0000250|UniProtKB:D4GZE7}.
STRAND 6 8 {ECO:0000244|PDB:5LDA}.
TURN 9 12 {ECO:0000244|PDB:5LDA}.
HELIX 25 31 {ECO:0000244|PDB:5LDA}.
TURN 36 38 {ECO:0000244|PDB:5LDA}.
STRAND 39 43 {ECO:0000244|PDB:5LDA}.
STRAND 46 48 {ECO:0000244|PDB:5LDA}.
STRAND 50 52 {ECO:0000244|PDB:1RWS}.
STRAND 60 64 {ECO:0000244|PDB:5LDA}.
SEQUENCE 69 AA; 7686 MW; BFDE8FF3EE8A7F15 CRC64;
MKMIKVKVIG RNIEKEIEWR EGMKVRDILR AVGFNTESAI AKVNGKVVLE DDEVKDGDFV
EVIPVVSGG


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